SitesBLAST
Comparing AO356_16720 AO356_16720 4-aminobutyrate aminotransferase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
43% identity, 99% coverage: 3:412/416 of query aligns to 11:420/425 of 1sffA
- active site: V18 (≠ I10), Y137 (≠ F129), E205 (= E197), D238 (= D230), Q241 (= Q233), K267 (= K259), T296 (= T288), R397 (= R389)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ N70), G110 (= G102), S111 (≠ A103), Y137 (≠ F129), H138 (= H130), R140 (= R132), E205 (= E197), D238 (= D230), V240 (≠ I232), Q241 (= Q233), K267 (= K259), T296 (= T288)
- binding sulfate ion: N152 (≠ A144), Y393 (≠ R385)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
43% identity, 99% coverage: 3:412/416 of query aligns to 11:420/425 of 1sf2A
- active site: V18 (≠ I10), Y137 (≠ F129), E205 (= E197), D238 (= D230), Q241 (= Q233), K267 (= K259), T296 (= T288), R397 (= R389)
- binding pyridoxal-5'-phosphate: G110 (= G102), S111 (≠ A103), Y137 (≠ F129), H138 (= H130), E205 (= E197), D238 (= D230), V240 (≠ I232), Q241 (= Q233), K267 (= K259)
- binding sulfate ion: N152 (≠ A144), Y393 (≠ R385)
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
43% identity, 99% coverage: 3:412/416 of query aligns to 12:421/426 of P22256
- I50 (= I41) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 102:103) binding
- E211 (= E202) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I232) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q233) binding
- K268 (= K259) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T288) binding
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
42% identity, 99% coverage: 3:412/416 of query aligns to 11:420/425 of 1szkA
- active site: V18 (≠ I10), Y137 (≠ F129), E205 (= E197), D238 (= D230), Q241 (= Q233), K267 (= K259), T296 (= T288), R397 (= R389)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G102), S111 (≠ A103), Y137 (≠ F129), H138 (= H130), E205 (= E197), D238 (= D230), V240 (≠ I232), Q241 (= Q233), K267 (= K259)
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
42% identity, 94% coverage: 22:413/416 of query aligns to 30:420/421 of P50457
- K267 (= K259) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
39% identity, 99% coverage: 6:415/416 of query aligns to 28:438/439 of 3q8nC
- active site: V32 (≠ I10), Y151 (≠ F129), E221 (= E197), D254 (= D230), Q257 (= Q233), K283 (= K259), T312 (= T288), R412 (= R389)
- binding 4-oxobutanoic acid: G124 (= G102), A125 (= A103), V256 (≠ I232), K283 (= K259)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
40% identity, 93% coverage: 28:414/416 of query aligns to 53:437/440 of 6j2vA
- active site: Y154 (≠ F129), D256 (= D230), K285 (= K259)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G102), A128 (= A103), Y154 (≠ F129), H155 (= H130), R157 (= R132), E223 (= E197), E228 (= E202), D256 (= D230), I258 (= I232), K285 (= K259), G313 (= G287), T314 (= T288)
Sites not aligning to the query:
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
41% identity, 96% coverage: 15:412/416 of query aligns to 40:441/444 of 4atqF
- active site: Y154 (≠ F129), E226 (= E197), D259 (= D230), Q262 (= Q233), K288 (= K259), T317 (= T288), R418 (= R389)
- binding gamma-amino-butanoic acid: M95 (≠ N70), Y154 (≠ F129), R157 (= R132), E231 (= E202), K288 (= K259), G316 (= G287)
- binding pyridoxal-5'-phosphate: G127 (= G102), A128 (= A103), Y154 (≠ F129), H155 (= H130), D259 (= D230), V261 (≠ I232)
Sites not aligning to the query:
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 99% coverage: 2:413/416 of query aligns to 15:395/395 of Q5SHH5
- GT 113:114 (≠ GA 102:103) binding
- K254 (= K259) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T288) binding
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 99% coverage: 2:413/416 of query aligns to 7:387/387 of 1wkhA
- active site: S13 (≠ Q8), F132 (= F129), E184 (= E197), D217 (= D230), Q220 (= Q233), K246 (= K259), T275 (= T288), R363 (= R389)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I41), S104 (= S101), G105 (= G102), T106 (≠ A103), F132 (= F129), S133 (≠ H130), E184 (= E197), E189 (= E202), D217 (= D230), I219 (= I232), K246 (= K259), R363 (= R389)
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 99% coverage: 2:413/416 of query aligns to 7:387/387 of 1wkgA
- active site: S13 (≠ Q8), F132 (= F129), E184 (= E197), D217 (= D230), Q220 (= Q233), K246 (= K259), T275 (= T288), R363 (= R389)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (≠ S11), Y46 (≠ I41), G105 (= G102), T106 (≠ A103), F132 (= F129), S133 (≠ H130), R135 (= R132), E184 (= E197), D217 (= D230), I219 (= I232), Q220 (= Q233), K246 (= K259), G273 (= G286), T274 (≠ G287), T275 (= T288)
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 99% coverage: 2:413/416 of query aligns to 7:387/387 of 1vefA
- active site: S13 (≠ Q8), F132 (= F129), D217 (= D230), K246 (= K259), T275 (= T288), R363 (= R389)
- binding pyridoxal-5'-phosphate: G105 (= G102), T106 (≠ A103), F132 (= F129), S133 (≠ H130), E184 (= E197), D217 (= D230), I219 (= I232), K246 (= K259)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
31% identity, 94% coverage: 18:409/416 of query aligns to 29:426/439 of 5wyaA
- active site: Y140 (≠ F129), E215 (= E197), D248 (= D230), N251 (≠ Q233), K278 (= K259), T307 (= T288), R406 (= R389)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I41), Y82 (≠ A71), S112 (= S101), G113 (= G102), S114 (≠ A103), Y140 (≠ F129), H141 (= H130), E215 (= E197), D248 (= D230), V250 (≠ I232), N251 (≠ Q233), K278 (= K259), F306 (≠ G287), T307 (= T288), R406 (= R389)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
31% identity, 94% coverage: 18:409/416 of query aligns to 38:435/448 of 4ysnC
- active site: Y149 (≠ F129), E224 (= E197), D257 (= D230), N260 (≠ Q233), K287 (= K259), T316 (= T288), R415 (= R389)
- binding pyridoxal-5'-phosphate: S121 (= S101), G122 (= G102), S123 (≠ A103), Y149 (≠ F129), H150 (= H130), E224 (= E197), D257 (= D230), V259 (≠ I232), K287 (= K259), F315 (≠ G287), T316 (= T288)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
31% identity, 94% coverage: 18:409/416 of query aligns to 31:428/446 of 5wyfA
- active site: Y142 (≠ F129), E217 (= E197), D250 (= D230), N253 (≠ Q233), K280 (= K259), T309 (= T288), R408 (= R389)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I41), Y84 (≠ A71), G115 (= G102), S116 (≠ A103), Y142 (≠ F129), H143 (= H130), D222 (≠ E202), D250 (= D230), V252 (≠ I232), N253 (≠ Q233), K280 (= K259), F308 (≠ G287), T309 (= T288), R408 (= R389)
Sites not aligning to the query:
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
31% identity, 95% coverage: 21:415/416 of query aligns to 26:398/402 of 4jevB
- active site: F136 (= F129), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T279 (= T288), R372 (= R389)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I41), S102 (= S101), G103 (= G102), T104 (≠ A103), F136 (= F129), H137 (= H130), E188 (= E197), E193 (= E202), D221 (= D230), V223 (≠ I232), Q224 (= Q233), K250 (= K259), R372 (= R389)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
34% identity, 94% coverage: 21:410/416 of query aligns to 26:393/400 of 4addA
- active site: F136 (= F129), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T279 (= T288), R372 (= R389)
- binding pyridoxal-5'-phosphate: G103 (= G102), A104 (= A103), F136 (= F129), H137 (= H130), D221 (= D230), V223 (≠ I232), K250 (= K259)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F129), R139 (= R132)
Sites not aligning to the query:
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
34% identity, 94% coverage: 21:410/416 of query aligns to 26:393/401 of 4adbB
- active site: F136 (= F129), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T279 (= T288), R372 (= R389)
- binding pyridoxal-5'-phosphate: S102 (= S101), G103 (= G102), A104 (= A103), F136 (= F129), H137 (= H130), D221 (= D230), V223 (≠ I232), Q224 (= Q233), K250 (= K259)
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
31% identity, 95% coverage: 21:415/416 of query aligns to 31:403/405 of P40732
- GT 108:109 (≠ GA 102:103) binding
- K255 (= K259) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T288) binding
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
32% identity, 96% coverage: 13:412/416 of query aligns to 23:409/412 of 2eo5A
- active site: F139 (= F129), E219 (= E197), D252 (= D230), Q255 (= Q233), K281 (= K259), T303 (= T288), R386 (= R389)
- binding pyridoxal-5'-phosphate: G113 (= G102), T114 (≠ A103), F139 (= F129), H140 (= H130), E219 (= E197), D252 (= D230), V254 (≠ I232), Q255 (= Q233), K281 (= K259)
Sites not aligning to the query:
Query Sequence
>AO356_16720 AO356_16720 4-aminobutyrate aminotransferase
MSSETISQSISIVHPVSLSHGRNAEVWDTDGKRYIDFVGGIGVLNLGHCHPRIVEAIREQ
ATRLTHYAFNAAPHAPYIELMERLAAFVPVDYPVSGMLTNSGAEAAENALKIVRGATGRT
AVIAFDGAFHGRTLATLNLNGKVAPYKQKVGVLPGPVYHLPYPSQDNGVTCAEALKAMER
LFSVEIDVNDVACFIVEPVQGEAGFLAMDVPFAQALRQFCDDKGIVLIIDEIQSGFGRTG
QRFAFSRLGIEPDLILLGKSIAGGVPLGAVVGRKALLDNLPKGGLGGTYSGNPIACAAAL
ATLDEMTDANLHAWGVQQQEAIVSRYESWRSRGLSPYLGRLTGIGAMRGIELSQADGTPA
SAQLTQLLALARESGLLLMPSGKSRHIVRLLAPLTTEPAVLEEGLDILEACLAKLA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory